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  • CDP-ethanolamine-(aminocaproyl)-agarose  (1)
  • proton driven transport  (1)
  • Springer  (2)
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  • Springer  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European journal of nutrition 30 (1991), S. 233-237 
    ISSN: 1436-6215
    Keywords: Hydroxyanaloga von Aminosäuren ; H+-Ionen-stimulierter Transport ; Bürstensaum-Membranvesikel ; hydroxy analogues of amino acids ; proton driven transport ; brushborder membran vesicles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Medicine
    Description / Table of Contents: Summary Hydroxy analogues of essential amino acids can be used in clinical nutrition to minimize nitrogen intake. In this study intestinal uptake of L-leucine hydroxy analogue into rabbit jejunal brush-border membrane vesicles was investigated. An inward directed H+-gradient was a driving force of uptake (pHoutside = 6.0; pHinside = 7.5) and led to a transient accumulation. The saturable system has a apparent transport constant Kt = 15.4 mM. By trans stimulation experiments it could be shown that both D- and L-stereoisomers of hydroxy analogues of branched chain amino acids as well as L-lactate share with the same H+-driven uptake system.
    Notes: Zusammenfassung Hydroxyanaloga essentieller Aminosäuren können ebenso wie ihre Ketoanaloga zur Minimierung der nutritiven Stickstoffaufnahme verwandt werden. In der vorliegenden Arbeit werden Mechanismen der intestinalen Absorption des L-Hydroxyanalogons von Leucin untersucht. Die Aufnahme dieses Substrates in Bürstensaum-Membranvesikel des jejunalen Kaninchendünndarms wird durch einen nach innen gerichteten Protonengradienten stimuliert (pHaußen 6,0; pHinnen 7,5). Die scheinbare Transportkonstante beträgt 15,4mM. Durch das carriervermittelte Transportsystem werden gleichfalls L- und D-Stereoisomere der anderen Hydroxyanaloga verzweigtkettiger Aminosäuren sowie L-Lactat aufgenommen.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4986
    Keywords: sialyltransferase ; colostrum ; CDP-ethanolamine-(aminocaproyl)-agarose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Cytidine-5′-monophospho-N-acetylneuraminic acid:β-galactoside α2-6sialyltransferase was purified from bovine colostrum by two sequential affinity chromatography steps on CDP-ethanolamine-Sepharose and CDP-ethanolamine-(N-caproylamino-)-Sepharose, respectively. While the conditions for elution were those of Paulsonet al. [J Biol Chem (1977) 252:3256–62], the ligand of the second affinity column was coupled to Sepharose by using 6-aminocaproic acid as linker. The ease of this procedure allows rapid synthesis of bulk quantities of ligand. Highly purified preparations of sialyltransferase were obtained which moved on gradient gel electrophoresis as a single band of 76 kDa and on dodecylsulphate electrophoresis as a single band of 54 kDa. The product of the reaction between lactose and CMP-N-acetylneuraminic acid catalyzed by the purified sialyltransferase was identified by high-resolution 500 MHz1H-NMR spectroscopy as Neu5Acα2-6Galβ1-4Glc.
    Type of Medium: Electronic Resource
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